APC13_HUMAN
ID APC13_HUMAN Reviewed; 74 AA.
AC Q9BS18; Q9Y3V0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Anaphase-promoting complex subunit 13;
DE Short=APC13;
DE AltName: Full=Cyclosome subunit 13;
GN Name=ANAPC13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=15060174; DOI=10.1128/mcb.24.8.3562-3576.2004;
RA Schwickart M., Havlis J., Habermann B., Bogdanova A., Camasses A.,
RA Oelschlaegel T., Shevchenko A., Zachariae W.;
RT "Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-
RT promoting complex stabilizing the association of Cdc16 and Cdc27.";
RL Mol. Cell. Biol. 24:3562-3576(2004).
RN [4]
RP IDENTIFICATION IN THE APC/C COMPLEX.
RX PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
RA Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
RA Engel A., Peters J.-M., Stark H.;
RT "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
RT cryo-electron microscopy model of vertebrate APC/C.";
RL Mol. Cell 20:867-879(2005).
RN [5]
RP FUNCTION OF THE APC/C.
RX PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
RA Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
RT "Mechanism of ubiquitin-chain formation by the human anaphase-promoting
RT complex.";
RL Cell 133:653-665(2008).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
RX PubMed=25043029; DOI=10.1038/nature13543;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Molecular architecture and mechanism of the anaphase-promoting complex.";
RL Nature 513:388-393(2014).
RN [7] {ECO:0007744|PDB:4UI9}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
RX PubMed=26083744; DOI=10.1038/nature14471;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Atomic structure of the APC/C and its mechanism of protein
RT ubiquitination.";
RL Nature 522:450-454(2015).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
CC {ECO:0000269|PubMed:15060174, ECO:0000269|PubMed:18485873}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5. {ECO:0000269|PubMed:16364912, ECO:0000269|PubMed:25043029,
CC ECO:0000269|PubMed:26083744}.
CC -!- INTERACTION:
CC Q9BS18; Q9UJX2: CDC23; NbExp=7; IntAct=EBI-2555953, EBI-396137;
CC Q9BS18; O76024: WFS1; NbExp=3; IntAct=EBI-2555953, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the APC13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43251.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AL050051; CAB43251.1; ALT_FRAME; mRNA.
DR EMBL; BC005398; AAH05398.1; -; mRNA.
DR CCDS; CCDS3085.1; -.
DR PIR; T08723; T08723.
DR RefSeq; NP_001229303.1; NM_001242374.1.
DR RefSeq; NP_001229304.1; NM_001242375.1.
DR RefSeq; NP_056206.1; NM_015391.3.
DR PDB; 4UI9; EM; 3.60 A; M=1-74.
DR PDB; 5G04; EM; 4.00 A; M=1-74.
DR PDB; 5KHR; EM; 6.10 A; M=1-74.
DR PDB; 5KHU; EM; 4.80 A; M=1-74.
DR PDB; 5L9T; EM; 6.40 A; M=1-74.
DR PDB; 5L9U; EM; 6.40 A; M=1-74.
DR PDB; 5LCW; EM; 4.00 A; M=1-74.
DR PDB; 6Q6G; EM; 3.20 A; M=1-74.
DR PDB; 6Q6H; EM; 3.20 A; M=1-74.
DR PDB; 6TLJ; EM; 3.80 A; M=1-74.
DR PDB; 6TM5; EM; 3.90 A; M=1-74.
DR PDB; 6TNT; EM; 3.78 A; M=1-74.
DR PDB; 7QE7; EM; 2.90 A; M=1-74.
DR PDBsum; 4UI9; -.
DR PDBsum; 5G04; -.
DR PDBsum; 5KHR; -.
DR PDBsum; 5KHU; -.
DR PDBsum; 5L9T; -.
DR PDBsum; 5L9U; -.
DR PDBsum; 5LCW; -.
DR PDBsum; 6Q6G; -.
DR PDBsum; 6Q6H; -.
DR PDBsum; 6TLJ; -.
DR PDBsum; 6TM5; -.
DR PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9BS18; -.
DR SMR; Q9BS18; -.
DR BioGRID; 117372; 82.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR DIP; DIP-56455N; -.
DR IntAct; Q9BS18; 23.
DR STRING; 9606.ENSP00000421842; -.
DR iPTMnet; Q9BS18; -.
DR PhosphoSitePlus; Q9BS18; -.
DR BioMuta; ANAPC13; -.
DR DMDM; 74732956; -.
DR EPD; Q9BS18; -.
DR jPOST; Q9BS18; -.
DR MassIVE; Q9BS18; -.
DR MaxQB; Q9BS18; -.
DR PaxDb; Q9BS18; -.
DR PeptideAtlas; Q9BS18; -.
DR PRIDE; Q9BS18; -.
DR ProteomicsDB; 78858; -.
DR Antibodypedia; 49243; 78 antibodies from 24 providers.
DR DNASU; 25847; -.
DR Ensembl; ENST00000354910.10; ENSP00000346987.5; ENSG00000129055.13.
DR Ensembl; ENST00000510994.5; ENSP00000421842.1; ENSG00000129055.13.
DR Ensembl; ENST00000511751.1; ENSP00000421760.1; ENSG00000129055.13.
DR Ensembl; ENST00000514612.5; ENSP00000427327.1; ENSG00000129055.13.
DR GeneID; 25847; -.
DR KEGG; hsa:25847; -.
DR MANE-Select; ENST00000354910.10; ENSP00000346987.5; NM_015391.4; NP_056206.1.
DR UCSC; uc003eqi.4; human.
DR CTD; 25847; -.
DR DisGeNET; 25847; -.
DR GeneCards; ANAPC13; -.
DR HGNC; HGNC:24540; ANAPC13.
DR HPA; ENSG00000129055; Low tissue specificity.
DR MIM; 614484; gene.
DR neXtProt; NX_Q9BS18; -.
DR OpenTargets; ENSG00000129055; -.
DR PharmGKB; PA134949652; -.
DR VEuPathDB; HostDB:ENSG00000129055; -.
DR eggNOG; ENOG502S4J1; Eukaryota.
DR GeneTree; ENSGT00390000008673; -.
DR HOGENOM; CLU_199969_0_0_1; -.
DR InParanoid; Q9BS18; -.
DR OMA; PHDDIAV; -.
DR OrthoDB; 1635284at2759; -.
DR PhylomeDB; Q9BS18; -.
DR TreeFam; TF105448; -.
DR PathwayCommons; Q9BS18; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9BS18; -.
DR SIGNOR; Q9BS18; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 25847; 336 hits in 1078 CRISPR screens.
DR ChiTaRS; ANAPC13; human.
DR GenomeRNAi; 25847; -.
DR Pharos; Q9BS18; Tbio.
DR PRO; PR:Q9BS18; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BS18; protein.
DR Bgee; ENSG00000129055; Expressed in nephron tubule and 215 other tissues.
DR ExpressionAtlas; Q9BS18; baseline and differential.
DR Genevisible; Q9BS18; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR InterPro; IPR008401; Apc13.
DR PANTHER; PTHR28672; PTHR28672; 1.
DR Pfam; PF05839; Apc13p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..74
FT /note="Anaphase-promoting complex subunit 13"
FT /id="PRO_0000253980"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 8
FT /note="D -> G (in Ref. 1; CAB43251)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="E -> G (in Ref. 1; CAB43251)"
FT /evidence="ECO:0000305"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 51..55
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:7QE7"
SQ SEQUENCE 74 AA; 8521 MW; F3C52A7E3821CB3B CRC64;
MDSEVQRDGR ILDLIDDAWR EDKLPYEDVA IPLNELPEPE QDNGGTTESV KEQEMKWTDL
ALQYLHENVP PIGN
